PDGF‐induced Akt phosphorylation does not activate NF‐κB in human vascular smooth muscle cells and fibroblasts

FEBS Letters

Rauch, Bernhard H.¹  Weber, Artur-Aron¹  Schrör, Karsten¹  Zimmermann, Norbert²  Braun, Marina¹ 

[1] Institut für Pharmakologie und Klinische Pharmakologie, Heinrich-Heine-Universität Düsseldorf, Moorenstr. 5, 40225 Düsseldorf, Germany;Klinik für Thorax- und Kardiovaskuläre Chirurgie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany

关键词: Nuclear factor-κB;    Akt phosphorylation;    Cytokine;    Growth factor;    Vascular smooth muscle cell;    EDTA;    ethylenediamine-tetraacetic acid;    IκB;    inhibitory protein κB;    NF-κB;    nuclear factor κB;    PBS;    phosphate-buffered saline;    PDGF;    platelet-derived growth factor;    SDS;    sodium dodecyl sulfate;    SMC;    smooth muscle cells;    TNFα;    tumor necrosis factor-α;   

DOI  :  10.1016/S0014-5793(00)01957-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A recent report suggested that platelet-derived growth factor (PDGF) activates nuclear factor-κB (NF-κB) by phosphorylation of the protein kinase Akt [Romashkova and Makarov, Nature 401 (1999) 86–90]. The present study investigates the role of Akt in the activation of NF-κB by tumor necrosis factor-α (TNFα, 10 ng/ml) and PDGF-BB (20 ng/ml) in human vascular smooth muscle cells (SMC), skin and foreskin fibroblasts. TNFα stimulated serine phosphorylation and degradation of the inhibitory protein IκBα and strongly induced nuclear NF-κB translocation and binding activity. PDGF did not induce serine phosphorylation or degradation of IκBα and did not enhance binding activity of NF-κB. In contrast, stimulation with PDGF resulted in a marked phosphorylation of Akt, but no Akt phosphorylation occurred after stimulation with TNFα. These data suggest that Akt phosphorylation is not involved in NF-κB activation in human SMC and fibroblasts.

【 授权许可】

Unknown